Effect of the Two Conserved Prolines of Human Growth Inhibitory Factor (Metallothionein-3) on Its Biological Activity and Structure Fluctuation:  Comparison with a Mutant Protein†

Biochemistry ◽  
2000 ◽  
Vol 39 (47) ◽  
pp. 14567-14575 ◽  
Author(s):  
Daniel W. Hasler ◽  
Laran T. Jensen ◽  
Oliver Zerbe ◽  
Dennis R. Winge ◽  
Milan Vašák
Keyword(s):  
Biological Activity ◽  
Human Growth ◽  
Inhibitory Factor ◽  
Mutant Protein ◽  
Growth Inhibitory Factor ◽  
Growth Inhibitory

scholarly journals TheΔ33-35 Mutantα-Domain Containingβ-Domain-LikeM3S9Cluster Exhibits the Function ofα-Domain withM4S11Cluster in Human Growth Inhibitory Factor

2010 ◽  
Vol 2010 ◽  
pp. 1-8
Author(s):  
Qingui Bao ◽  
Zhichun Ding ◽  
Zhong-Xian Huang ◽  
Xiangshi Tan
Keyword(s):  
Inhibitory Activity ◽  
Solvent Accessibility ◽  
Human Growth ◽  
Biochemical Properties ◽  
Inhibitory Factor ◽  
Neuronal Growth ◽  
Domain Interaction ◽  
Ph Titration ◽  
Growth Inhibitory Factor ◽  
Growth Inhibitory

Neuronal growth inhibitory factor (GIF), also known as metallothionein (metallothionein-3), impairs the survival and neurite formation of cultured neurons. It is known that theα-βdomain-domain interaction of hGIF is crucial to the neuron growth inhibitory bioactivity although the exact mechanism is not clear. Herein, theβ(MT3)-β(MT3) mutant and the hGIF-truncatedΔ33-35 mutant were constructed, and their biochemical properties were characterized by pH titration, EDTA, and DTNB reactions. Their inhibitory activity toward neuron survival and neurite extension was also examined. We found that theΔ33-35 mutantα-domain containingβ-domain-likeM3S9cluster exhibits the function ofα-domain withM4S11cluster in hGIF. These results showed that the stability and solvent accessibility of the metal-thiolate cluster inβ-domain is very significant to the neuronal growth inhibitory activity of hGIF and also indicated that the particular primary structure ofα-domain is pivotal to domain-domain interaction in hGIF.

scholarly journals Could a Growth Inhibitory Factor, Present Only during Pregnancy, be Made Available to Treat Cancer in Adults? A Commentary

2021 ◽  
Vol 6 (1) ◽  
Author(s):  
Mizejewski GJ
Keyword(s):  
Fetal Growth ◽  
Therapeutic Agent ◽  
Germ Cell Tumors ◽  
Inhibitory Factor ◽  
Additional Function ◽  
Major Function ◽  
Growth Inhibitory Factor ◽  
Growth Inhibitory ◽  
Age Dependent ◽  
Growth Promoting

Human alpha-fetoprotein (AFP) is well-known as the “gold standard” biomarker for liver and germ cell tumors. It has also been utilized as a pregnancy screening analyte for neural tube defects as well as Down syndrome, when combined with other gestational-age dependent biomarkers. However, a lesser known and recognized property of AFP is its role in the maintenance and monitoring of fetal growth during ontogenetic development in man. Although a major function of AFP during pregnancy involves the serum transport of estrogens, fatty acids, retinoid, and other compounds, the positive and negative regulation of fetal growth is a vital additional function of AFP. Human AFP largely functions as a growth promoting agent; however, the fetal protein is able to temporarily convert to a growth inhibitory factor in stress and shock environments in the fetal milieu. The development of a transient form of AFP or its derived peptides could be harnessed for use as an adjunct therapeutic agent to treat cancer in adults.

Normal mouse lung tissue produces a growth-inhibitory factor(s) preferential for mouse monocytic leukemia cells

1989 ◽  
Vol 30 (3) ◽  
pp. 139-144 ◽  
Author(s):  
Togo Ikuta ◽  
Yoshio Honma ◽  
Junko Okabe-Kado ◽  
Takashi Kasukabe ◽  
Motoo Hozumi
Keyword(s):  
Lung Tissue ◽  
Normal Mouse ◽  
Inhibitory Factor ◽  
Leukemia Cells ◽  
Mouse Lung ◽  
Monocytic Leukemia ◽  
Growth Inhibitory Factor ◽  
Growth Inhibitory ◽  
Mouse Lung Tissue
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